Abstract
A chimeric enzyme based on the genetic fusion of a laccase with a hydrophobin domain was employed to functionalize few-layer graphene, previously exfoliated from graphite in the presence of the hydrophobin. The as-produced, biofunctionalized few-layer graphene was characterized by electrochemistry and Raman spectroscopy, and finally employed in the biosensing of phenols such as catechol and dopamine. This strategy paves the way for the functionalization of nanomaterials by hydrophobin domains of chimeric enzymes and their use in a variety of electrochemical applications.
Highlights
Graphene is a two-dimensional sheet of sp2-hybridized carbon that exhibits unparalleled properties such as high planar surface, superlative mechanical strength, and remarkable thermal and electrical conductivity
chemical vapor deposition (CVD) produces a large surface of monolayer graphene, soft exfoliation of graphite has been able to provide low-cost access to few-layer graphene (FLG) dispersions
Vmh2-exfoliated graphene is generally stable in 60% ethanol (EtOH) thanks to the presence of the HFB
Summary
Graphene is a two-dimensional sheet of sp2-hybridized carbon that exhibits unparalleled properties such as high planar surface, superlative mechanical strength, and remarkable thermal and electrical conductivity. Graphene acts as a conductive platform for biomolecule immobilization and electrochemical detection of bioanalytes [9,10,11,12,13,14]. Different techniques have been investigated for the production of graphene such as scotch-tape transfer, chemical vapor deposition (CVD) growth, and chemically or electrochemically reduced graphene oxide. These strategies lead to different nanomaterials in terms of size, edge and basal defects, number of layers, and oxygenated defect content. Graphene is a very suitable platform for enzyme immobilization thanks to its high surface area, dispersion in solution, and tunable surface chemistry. The hydrophobic interactions driving the direct immobilization of active proteins on graphene surface are often difficult to achieve, and modifications of the protein
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